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Enzymology Project Assessment Answer

Enzymology Project

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Abstract

Enzymology is a field where a wide number of issues and problems can be benefitted from a computational approach. While many challenges remain in quantitative prediction behavior for different enzyme systems, the parameters that often come from computations are a necessary criterion for the enzymology community. In this article, we will provide you how enzymologists over different types of calculations that are extremely useful for problems in enzymology. Particularly, the enzymologists emphasize the process of integration of models that varies from small active-site motifs to entirely solvated enzyme systems for dissection and cross-validation of the contributions from the environment of enzymes. The case study of alkaline phosphatase is used for the illustration of a specific application of different methods. The analysis includes the examination process of the binding patterns of putative transition state analogs to the enzyme. The computational methods for the prediction of covalent bonds involved in the interactions of these ions to the enzymatic nucleophile and they go through the adoption process of the trigonal bipyramidal geometry of the transition state expected. By the comparative study of the structures of the enzymes along with the transition, states are found through free energy simulations the assessment of the degree to which the analogs of the transition state mimic the true transition states. The technical issues are worth treating the care and several challenges to the quantitative analysis of metalloenzymes are also highlighted in the ongoing discussion. Carboxypeptidases are involved in various types of physiological modes by the removal of C-terminal amino acids from peptidases and protein. Few of the carboxypeptidase's function in the degradation of the protein in the digestive pipe, while the different enzyme plays a synthetic role in the formation of peptide and neuropeptide hormones. The other set of carboxypeptidases contributes to the modification of tubulin by the removal of amino acids from the C terminus and by the side chain of polyglutamic followed by the alteration of the microtubule's properties. The review majorly focuses on major types of carboxypeptidases, types of enzymes, and enzyme kinetics. The natural mutation takes place majorly three types of enzymes associated along with the disease phenotypes that range from epilepsy to neurodegeneration. The major application tool which is known as peptidomes is used for the investigation of the relation among the alteration and mutations in the levels of a peptide. The methods id applied for the definition of the characteristics and function of enzymes. The studies help elucidate the function of enzymes for the clarification of the biological pinning of pathological by the identification of the peptide altered in the state of diseases. The review will help you in the application of peptidomes-based techniques for gaining exposure to the normal function of enzymes and the molecular defects which is caused by the mutation in enzymes. The enzymes perform various types of functions in the body. A catalyst is a substance that affects the rate of a reaction without considering permanent changes or consumption in the reaction. Catalysts in the biological systems belong to a special division of proteins called enzymes. The substrate is known as the substance upon which the enzyme is operated.

Introduction

An Enzymology is an effective branch of biochemistry that mainly aims to effectively get able to understand how enzymes work through having several relationships between both the function and the structure and how they effectively get fold in the native state. It is an effective study of the enzymes. The kinetics substrate data had been effectively getting demonstrated with the help of properly defining this with some of the empirical equations that are mainly get related to the kinetic data of ten substrates that consists of both peptides and esters and which having sigmoid and inhibition. It mainly helps in effectively speeding up some effective chemical reactions in the body of human beings. They are mainly necessary for effective respiration in the human body, effective digestion of food in the body, and some other related functions of the human body. They generally get builds from proteins and are present almost everywhere. It effectively helps the body to break down the larger molecules into smaller ones Enzymes could effectively work in certain specific conditions and if it would get the lowest temperature then it would perform its work so slowly and if the temperature is high then it would be more acidic so due to this certain condition must get exists so that the enzymes could effectively work properly.

Classification for enzyme

A major and effective classification of enzymes generally get consists of hydrolases, ligases, mutases, desmolases, and the polysaccharide and the synthesizing enzymes. Cofactor could effectively get sub-divided into the two major categories that are small organic molecules and the metals as the cofactors are the small carbon-based particles and generally get considered as the coenzymes and cofactors are also get referred to as the prosthetic groups. An enzyme is a catalyst that effectively helps in increasing the velocity of the chemical reaction without effectively going under the long-lasting chemical change. The major reaction of the enzymes could be effectively get presented as E- that mainly represent the reaction of catalyst of the enzyme, S- it is the substrate which gets effectively changed P- it is the product of the reaction and the effective mechanism of the enzyme could be effectively get described with the two parameters that are the thermodynamic changes and the major process for some active sites.

The Lipscomb generally offers an effective resolution for the disparity that is between the several interpretation models that had been interpreted earlier and the structural data and between the various substrate dynamic data. At the active center, there are mainly five major categories of the substrate molecules and the two sites related to this one is the catalyst and the other one is inhibitory. Richards and Quiocho have been effectively given the general model and that is the enzyme’s monomeric form that effectively gets requirement for three up to five substrates’ molecules for the process of inhibition. Several basic of the enzymology has been effectively getting consists of the development of activity essays and various purifications. Co enzymes generally get consist of water resolvable vitamins and which could effectively function as the substrate and the prosthetic group. Enzyme inhibition gets to consists of Competitive, and non-competitive inhibition, suicide, and allosteric inhibition. For the binding substrate, the active site is the carboxypeptidase, and this process is generally get considered as the induced fit and the model for the induced fit was given by the Koshland in this several water molecules and the side chain is effectively get displaced with each other.

Metallocarboxypeptidases

This is effective and important zinc that are mainly a dependent enzyme that mainly divides the single amino acid in the C- terminal of the peptide and into the protein and it effectively gets contribute into the wide variety of the physiological process in human that mainly gets range between the process from the effective digestion of protein for the effective blood regulation and the proper maturing of neuropeptides and also of hormones as per the database of Merope the most studied group for this is the MCP family and the proteases family and based on the homologies and the structural features the larger family could effectively get grouped into the ABCD and it effectively get consists of the subfamilies of carboxypeptidase. The effective feature of this zymogen is the availability of elevation and the Prodo main and all this had been effectively blocking their activities that are mainly get related to the catalysts.

Enzyme Kinetics

In the field of enzymology which is a vast and detailed topic of science, enzyme kinetics forms the influential and important part. By the definition, Enzyme Kinetics is the field of biochemistry which is majorly concerned with the measurements and the calculations of the reactions that consume enzyme and certain catalysts. During a reaction, it is already known that without even participating in the reaction catalysts affect the rate of reaction. Either it alters the speed of reaction by making it fast or slow or sometimes maintains the temperature too. Hence it is through Enzyme Kinetics where the learner learns regarding the measurements of the reaction. The rate of any reaction is measured and known by the number of molecules that are participating in the reaction. The number of molecules of the reactant that are finally converted to the product after a certain reaction in a given period. The rate of the reaction is always dependent upon the concentration of the chemicals that are participating in the process which is the reaction. The enzyme activity in the reaction is measured by the increase in the rate of reactions, under the conditions which are suitable for the reaction. For any reaction to happen there are certain conditions which include temperature, molecules, catalyst, and many more. The catalyst action of an enzyme is measured by a certain formula and there is a process that must be followed before reaching the result for such reactions. Thus, the catalytic action is measured by the difference between the turnover of catalyzed reaction and uncatalyzed reaction in the given time interval. The reaction rate is expressed by the change in the concentration per unit of time (mol 1 -1 s-1). Another point of interesting fact is that the enzyme activity is not dependent on the volume and the unit which is used for the same is katal (kat, mol s-1). The international unit differs by this and the international unit is µmol turnover min -1.

Factors affecting the Enzyme Kinetics

The factors that affect the Enzyme kinetics are the temperature of the reaction rate. The reaction rate of the reaction increases with the temperature it has been observed by the observer, and then at last declines with the temperature. In the case of the enzymes of animals, their enzymes become denatured above the temperature of 40 degrees Celsius. The temperature of the enzyme reactions for the higher organisms is usually counted as 50 degrees Celsius. The Q10 is also called the temperature coefficient. It is the temperature coefficient is the rate of a biological process it usually increases at the rate of 10 degrees Celsius.

Another factor is the effect of the potential hydrogen which is also known as the pH level of the enzyme activity. The rate of almost all of the enzyme-catalyzed reactions shows the dependence on hydrogen and the concentration of the ion. The pH value of the enzyme is between 5 and 9. The relationship between the potential hydrogen ion concentration shows the denaturation of enzymes at a high or a low level of ph.

Concentration of enzyme

It is observed that when the amount of enzyme is increased then the rate of reaction increases. This is a general trend. It is also observed that if the amount or the concentration of enzyme is increased more than it is required then the extra enzyme will not help in increasing the rate of reaction. Thus, to conclude the effect of the concentration of enzyme on reaction then it can be conferred that enzyme concentration increases at a certain point but then it levels off the reaction.

Conclusion

As per the report prepared for the enzyme and the activities related to the involvement of enzyme that various enzymes are responsible for the reactions that took place. Enzymes are found in humans and are also produced externally. They could be harmful as well as beneficial. The harmful enzyme contributes to the degrading of the metabolism and the reverse is also possible. As per the reaction with the enzyme is considered certain factors affect the reaction. The rate of any reaction is measured and known by the number of molecules that are participating in the reaction. The number of molecules of the reactant that are finally converted to the product after a certain reaction in a given period. The rate of the reaction is always dependent upon the concentration of the chemicals that are participating in the process which is the reaction. Catalysts promote the speed of reaction for enzymes and the measurement of reaction has different units. Studying enzymes requires a lot of research because it is a vast topic of science.

References

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  2. Sapio, M. R., & Fricker, L. D. (2014). Carboxypeptidases in disease: insights from peptidomics studies. Clinical applications, 8(5-6), 327–337. https://doi.org/10.1002/prca.201300090
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  9. Bu, H. (2006). A Literature Review of Enzyme Kinetic Parameters for CYP3A4-Mediated Metabolic Reactions of 113 Drugs in Human Liver Microsomes: Structure- Kinetics Relationship Assessment. Current Drug Metabolism, 7(3), 231-249. https://doi.org/10.2174/138920006776359329
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